3FWE
Crystal Structure of the Apo D138L CAP mutant
Summary for 3FWE
| Entry DOI | 10.2210/pdb3fwe/pdb |
| Descriptor | Catabolite gene activator, PROLINE (3 entities in total) |
| Functional Keywords | helix-turn-helix, transcription, camp, allostery, acetylation, activator, camp-binding, dna-binding, nucleotide-binding, transcription regulation, transcription regulator |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 2 |
| Total formula weight | 47571.28 |
| Authors | Sharma, H.,Wang, J.,Kong, J.,Yu, S.,Steitz, T. (deposition date: 2009-01-17, release date: 2009-09-08, Last modification date: 2024-02-21) |
| Primary citation | Sharma, H.,Yu, S.,Kong, J.,Wang, J.,Steitz, T.A. Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding Proc.Natl.Acad.Sci.USA, 106:16604-16609, 2009 Cited by PubMed Abstract: The binding of cAMP to the Escherichia coli catabolite gene activator protein (CAP) produces a conformational change that enables it to bind specific DNA sequences and regulate transcription, which it cannot do in the absence of the nucleotide. The crystal structures of the unliganded CAP containing a D138L mutation and the unliganded WT CAP were determined at 2.3 and 3.6 A resolution, respectively, and reveal that the two DNA binding domains have dimerized into one rigid body and their two DNA recognition helices become buried. The WT structure shows multiple orientations of this rigid body relative to the nucleotide binding domain supporting earlier biochemical data suggesting that the inactive form exists in an equilibrium among different conformations. Comparison of the structures of the liganded and unliganded CAP suggests that cAMP stabilizes the active DNA binding conformation of CAP through the interactions that the N(6) of the adenosine makes with the C-helices. These interactions are associated with the reorientation and elongation of the C-helices that precludes the formation of the inactive structure. PubMed: 19805344DOI: 10.1073/pnas.0908380106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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